5TZN
Structure of the viral immunoevasin m12 (Smith) bound to the natural killer cell receptor NKR-P1B (B6)
Summary for 5TZN
| Entry DOI | 10.2210/pdb5tzn/pdb |
| Descriptor | Killer cell lectin-like receptor subfamily B member 1B allele B, Glycoprotein family protein m12, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total) |
| Functional Keywords | c-type lectin-like domain, immonoglobulin like domain, cell invasion, immune system-viral protein complex, immune system/viral protein |
| Biological source | Mus musculus (Mouse) More |
| Total number of polymer chains | 4 |
| Total formula weight | 76910.84 |
| Authors | Berry, R.,Rossjohn, J. (deposition date: 2016-11-22, release date: 2017-05-24, Last modification date: 2024-10-16) |
| Primary citation | Aguilar, O.A.,Berry, R.,Rahim, M.M.,Reichel, J.J.,Popovic, B.,Tanaka, M.,Fu, Z.,Balaji, G.R.,Lau, T.N.,Tu, M.M.,Kirkham, C.L.,Mahmoud, A.B.,Mesci, A.,Krmpotic, A.,Allan, D.S.,Makrigiannis, A.P.,Jonjic, S.,Rossjohn, J.,Carlyle, J.R. A Viral Immunoevasin Controls Innate Immunity by Targeting the Prototypical Natural Killer Cell Receptor Family. Cell, 169:58-71.e14, 2017 Cited by PubMed Abstract: Natural killer (NK) cells play a key role in innate immunity by detecting alterations in self and non-self ligands via paired NK cell receptors (NKRs). Despite identification of numerous NKR-ligand interactions, physiological ligands for the prototypical NK1.1 orphan receptor remain elusive. Here, we identify a viral ligand for the inhibitory and activating NKR-P1 (NK1.1) receptors. This murine cytomegalovirus (MCMV)-encoded protein, m12, restrains NK cell effector function by directly engaging the inhibitory NKR-P1B receptor. However, m12 also interacts with the activating NKR-P1A/C receptors to counterbalance m12 decoy function. Structural analyses reveal that m12 sequesters a large NKR-P1 surface area via a "polar claw" mechanism. Polymorphisms in, and ablation of, the viral m12 protein and host NKR-P1B/C alleles impact NK cell responses in vivo. Thus, we identify the long-sought foreign ligand for this key immunoregulatory NKR family and reveal how it controls the evolutionary balance of immune recognition during host-pathogen interplay. PubMed: 28340350DOI: 10.1016/j.cell.2017.03.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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